3JZ7

Crystal structure of the extracellular domains of coxsackie & adenovirus receptor from mouse (mCAR)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	110
Detector technology	CCD
Collection date	2008-07-16
Detector	RAYONIX MX-225
Wavelength(s)	0.9184
Spacegroup name	P 21 21 2
Unit cell lengths	53.369, 61.468, 86.355
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.190
R-factor	0.212
Rwork	0.209
R-free	0.26500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1EAJ (complete) for domain D1 2V5R (residues 5-40 44-62 68-76 81-90) for domain D2
RMSD bond length	0.016
RMSD bond angle	1.483
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER (1.3.3)
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.260
High resolution limit [Å]	2.180	2.180
Rmerge	0.083	0.453
Number of reflections	15245
<I/σ(I)>	13.63	2.37
Completeness [%]	99.1	98.2
Redundancy	3.3	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293.15	protein buffer: 20mM TRIS 50mM NaCl protein concentration: 8mg / ml; crystallization buffer 0.1M HEPES pH 7.5 21% PEG 4000 15% isopropanol; crystalliztion setup: mixture 400nl protein sample : 400nl crystallization buffer reservoir filled with 80 ul crystallization buffer; cryo solution: 25% PEG 4000 20% isopropanol 10% glycerol 0.1M HEPES pH 7.5 freezing of crystals: crystallization setup was overlayed with cryosolution, floating crystals were removed with a cryoloop and flash-frozen in liquid nitrogen., VAPOR DIFFUSION, SITTING DROP, temperature 293.15K